Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 8001 |
| Chain | Residue |
| A | GLY154 |
| A | PHE155 |
| A | LYS270 |
| A | SER372 |
| A | THR373 |
| A | HOH2006 |
| A | HOH2021 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE VIN A 6331 |
| Chain | Residue |
| A | PHE155 |
| A | VAL158 |
| A | ALA169 |
| A | LYS171 |
| A | MET220 |
| A | GLU221 |
| A | ALA223 |
| A | ARG224 |
| A | GLY226 |
| A | ARG230 |
| A | SER272 |
| A | LEU275 |
| A | THR293 |
| A | ASP294 |
| A | ILE150 |
| A | GLY151 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 22 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGIGGFGKVYrAfwigde............VAVK |
| Chain | Residue | Details |
| A | ILE150-LYS171 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKssNILI |
| Chain | Residue | Details |
| A | ILE264-ILE276 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"15610029","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | SER272 | |
| A | ASP268 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP268 | |
| A | LYS270 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN273 | |
| A | ASP268 | |
| A | LYS270 | |
